지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
초록· 키워드
오류제보하기
Heat shock protein 90 (Hsp90) is a ubiquitous molecular chaperone, which is associated with stabilization of many oncogenic proteins for cancer cell survival. Hsp90 is overexpressed 2-10 fold higher in cancer cells than normal cells. Due to its potential to simultaneously disable multiple signaling pathway, Hsp90 has been identified as a validated target for cancer therapy. Accordingly, we designed and synthesized 2',4'-dimethoxychalcone derivatives to inhibit Hsp90 chaperone function. Among 2',4'-dimethoxychalcone derivatives, we found that compound 1g disrupted Hsp90 chaperoning function and impaired the growth of cancer cells. These findings indicated that 1g could serve a potential lead compound to target Hsp90 in cancer chemotherapy.
목차
등록된 정보가 없습니다.
참고문헌 (21)
참고문헌 신청
Young, J. C / 2000 / Polypeptide release by Hsp90involves ATP hydrolysis and is enhanced by the co-chaperone p23 / EMBO J 19:5930
Sun, J / 2015 / Synthesis and biological evaluation of 6,5-disubstituted-4-alkynylisoxozales as a novel class of HSP90inhibitors / Bioorg. Med. Chem. Lett 25:3129
Raman, S / 2015 / First structural view of a peptide interacting with the nucleotide binding domain of heat shock protein 90 / Sci. Rep 5:17015
Mahalingam, D / 2009 / Targeting HSP90 for cancer therapy / Br. J. Cancer 100:1523
Hanahan, D / 2000 / The hallmarks of cancer cell / Cell 100:57
Sun, J / 2015 / Synthesis and biological evaluation of 6,5-disubstituted-4-alkynylisoxozales as a novel class of HSP90inhibitors / Bioorg. Med. Chem. Lett 25:3129
Raman, S / 2015 / First structural view of a peptide interacting with the nucleotide binding domain of heat shock protein 90 / Sci. Rep 5:17015
Mahalingam, D / 2009 / Targeting HSP90 for cancer therapy / Br. J. Cancer 100:1523
Hanahan, D / 2000 / The hallmarks of cancer cell / Cell 100:57
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